Interleukin 3

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Interleukin 3 (colony-stimulating factor, multiple)
Identifiers
Symbols IL3; IL-3; MCGF; MGC79398; MGC79399; MULTI-CSF
External IDs OMIM147740 HomoloGene47938 GeneCards: IL3 Gene
RNA expression pattern
PBB GE IL3 207906 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3562 16187
Ensembl ENSG00000164399 ENSMUSG00000018914
UniProt P08700 P01586
RefSeq (mRNA) NM_000588.3 NM_010556
RefSeq (protein) NP_000579.2 NP_034686
Location (UCSC) Chr 5:
131.4 – 131.4 Mb
Chr 11:
54.08 – 54.08 Mb
PubMed search [1] [2]

Interleukin 3, also known as IL-3, is a protein that in humans is encoded by the IL3 gene.[1][2]

Contents

[edit] Function

Interleukin-3 (IL-3) is an interleukin, a type of biological signal (cytokine) that can improve the body's natural response to disease as part of the immune system. It acts by binding to the interleukin-3 receptor.

IL-3 stimulates the differentiation of multipotent hematopoietic stem cells into myeloid progenitor cells (as opposed to lymphoid progenitor cells where differentiation is stimulated by IL-7) as well as stimulates proliferation of all cells in the myeloid lineage (erythrocytes, megakaryocytes, granulocytes, monocytes, and dendritic cells). It is secreted by basophils and activated T cells to support growth and differentiation of T cells from the bone marrow in an immune response. The human IL-3 gene encodes a protein 152 amino acids long, and the naturally occurring IL-3 is glycosylated. The human IL-3 gene is located on chromosome 5, only 9 kilobases from the GM-CSF gene, and its function is quite similar to GM-CSF.

[edit] Discovery

Interleukin-3 originally was discovered by JN Ihle in mice. He found a T cell derived factor that induced the synthesis of 20alpha-hydroxysteroid dehydrogenase in hematopoietic cells and termed it interleukin-3.[3][4]

[edit] Interactions

Interleukin 3 has been shown to interact with IL3RA.[5][6]

[edit] See also

[edit] References

  1. ^ "Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3562. 
  2. ^ Yang YC, Ciarletta AB, Temple PA, Chung MP, Kovacic S, Witek-Giannotti JS, Leary AC, Kriz R, Donahue RE, Wong GG (October 1986). "Human IL-3 (multi-CSF): identification by expression cloning of a novel hematopoietic growth factor related to murine IL-3". Cell 47 (1): 3–10. doi:10.1016/0092-8674(86)90360-0. PMID 3489530. 
  3. ^ Ihle JN, Pepersack L, Rebar L (June 1981). "Regulation of T cell differentiation: in vitro induction of 20 alpha-hydroxysteroid dehydrogenase in splenic lymphocytes from athymic mice by a unique lymphokine". J. Immunol. 126 (6): 2184–9. PMID 6971890. http://www.jimmunol.org/cgi/content/abstract/126/6/2184. 
  4. ^ Ihle JN, Weinstein Y, Keller J, Henderson L, Palaszynski E (1985). "Interleukin 3". Meth. Enzymol.. Methods in Enzymology 116: 540–552. doi:10.1016/S0076-6879(85)16042-8. ISBN 9780121820169. PMID 3003517. 
  5. ^ Stomski, F C; Sun Q, Bagley C J, Woodcock J, Goodall G, Andrews R K, Berndt M C, Lopez A F (Jun. 1996). "Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding". Mol. Cell. Biol. (UNITED STATES) 16 (6): 3035–46. ISSN 0270-7306. PMC 231298. PMID 8649415. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231298. 
  6. ^ Woodcock, J M; Zacharakis B, Plaetinck G, Bagley C J, Qiyu S, Hercus T R, Tavernier J, Lopez A F (Nov. 1994). "Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF". EMBO J. (ENGLAND) 13 (21): 5176–85. ISSN 0261-4189. PMC 395466. PMID 7957082. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=395466. 

[edit] Further reading



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